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0518_4 Fission yeast Paa1 interactome

ABSTRACT: We performed mass-spectrometry analysis of proteins co-purifying with the Paa1, the structural subunit of the PP2A protein phosphatase complex. Paa1 was tagged with YFP at the C-terminus and expressed from its endogenous promoter at its chromosomal locus. After one hour of nitrogen starvation, Paa1-YFP was pulled down and co-purifying proteins were analysed by mass-spectrometry. Our results revealed the presence of all components of PP2A protein complexes including Paa1, the catalytic subunits Ppa1, Ppa2, and Ppa3, and the regulatory subunits Pab1, Par1 and Par2. Additionally, several PP2A regulators (Igo1, Zds1, Dis2, Ppe1 and Ekc1) and components of the PP2A SIP/STRIPAK complex were also detected, confirming that the pull-down approach was successful. The mass-spectrometry analysis also showed an over-representation of proteins related to ribosome structure, translation initiation, aminoacylation, and tRNA modification in the Paa1 interactome. We focused on Trm112, a widely conserved protein with a crucial role in translation.

INSTRUMENT(S): Bruker Daltonics timsTOF series

ORGANISM(S): Schizosaccharomyces Pombe

SUBMITTER: Sergio Moreno

LAB HEAD: Sergio Moreno

PROVIDER: PXD047703 | Pride | 2024-12-02

REPOSITORIES: Pride

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			Action	DRS
	0518_2_2_Slot1-37_1_3847.d.zip	Other
	0518_3_2_Slot1-38_1_3850.d.zip	Other
	0518_4_2_Slot1-39_1_3859.d.zip	Other
	0518_5_2_Slot1-40_1_3854.d.zip	Other
	0518_Supplementary_Table_3.xlsx	Xlsx

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